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Titolo:
STUDIES ON THE LIQUID-GLASS TRANSITION OF PROTEINS AND THEIR STRUCTURAL-CHANGES BY SITE-SELECTIVE FLUORESCENCE
Autore:
KUSHIDA T; KANEMATSU Y; KURITA A;
Indirizzi:
OSAKA UNIV,GRAD SCH SCI,DEPT PHYS,1-1 MACHIKANEYAMA TOYONAKA OSAKA 560 JAPAN
Titolo Testata:
Kobunshi ronbunshu
fascicolo: 10, volume: 53, anno: 1996,
pagine: 614 - 627
SICI:
0386-2186(1996)53:10<614:SOTLTO>2.0.ZU;2-3
Fonte:
ISI
Lingua:
JPN
Soggetto:
ZN-SUBSTITUTED MYOGLOBIN; INELASTIC NEUTRON-SCATTERING; DYE-DOPED POLYMERS; DENSITY-OF-STATES; MOLECULAR-DYNAMICS; VIBRATIONAL-MODES; SPECTROSCOPY; METMYOGLOBIN; CRYSTALS; BEHAVIOR;
Keywords:
PROTEIN DYNAMICS; MYOGLOBIN; GLASS; CONFORMATIONAL SUBSTATES; WEIGHTED DENSITY OF STATES; SITE-SELECTIVE FLUORESCENCE; HOLE BURNING;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
39
Recensione:
Indirizzi per estratti:
Citazione:
T. Kushida et al., "STUDIES ON THE LIQUID-GLASS TRANSITION OF PROTEINS AND THEIR STRUCTURAL-CHANGES BY SITE-SELECTIVE FLUORESCENCE", Kobunshi ronbunshu, 53(10), 1996, pp. 614-627

Abstract

Recent investigations of protein dynamics performed by the authors using laser spectroscopic techniques are reviewed. The site-selective fluorescence spectroscopy in zinc-substituted myoglobin has revealed that its absorption spectrum is inhomogeneously broadened at liquid helium temperature. The obtained data have enabled the extraction of the density of low-energy vibrational modes weighted by the electron-vibration coupling strengths. The absorption spectra below and above 180 K have been found to be reproduced by simulations under the assumptions offrozen and thermalized distributions among the conformational substates, respectively, in the ground state. This result supports the view that myoglobin molecules show a liquid-glass transition around 180 K. From the time-resolved measurements of resonance fluorescence spectra and hole spectra, it has also been found that a protein molecule exhibits a peculiar structural relaxation dynamics, which is quite differentfrom those in dye solutions. Information on the distribution of barrier heights separating the conformational substates and local structural change within a protein molecule has been obtained from the studies of the effect of temperature-cycling on the hole spectra burned at lowtemperatures. Recent trends of experimental studies on the conformational changes related to the liquid-glass transition of proteins are also discussed.

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Documento generato il 01/12/20 alle ore 19:44:59